The endosomal sorting complex required for transport (ESCRT) complexes form
the machinery driving protein sorting from endosomes to lysosomes. ESCRT
complexes are central to receptor downregulation, lysosome biogenesis, and
budding of HIV. Yeast ESCRT-I consists of three protein subunits, VPS23,
VPS28, and VPS37. In humans, ESCRT-I comprises TSG101, VPS28, and one of four
potential human VPS37 homologs. The main role of ESCRT-I is to recognize
ubiquitinated cargo via the UEV domain of the VPS23/TSG101 subunit. The
assembly of the ESCRT-I complex is directed by the C-terminal steadiness box
(SB) of VPS23, the N-terminal half of VPS28, and the C-terminal half of VPS37.
The structure is primarily composed of three long, parallel helical hairpins,
each corresponding to a different subunit (see <PDB:2CAZ>). The additional
domains and motifs extending beyond the core serve as gripping tools for
ESCRT-I critical functions [1,2].

The profiles we developed cover the entire steadiness box, VPS28 N-terminal
and VPS37 C-terminal domains.

Last update:

May 2007 / First entry.

Technical section

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